Source:http://linkedlifedata.com/resource/pubmed/id/19138084
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2009-2-4
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pubmed:abstractText |
Soybeans are recognized as one of the "big 8" food allergens. IgE antibodies from soybean-sensitive patients recognize more than 15 soybean proteins. Among these proteins only the alpha-subunit of beta-conglycinin, but not the highly homologous alpha'- and beta-subunits, has been shown to be a major allergenic protein. The objective of this study was to examine if the alpha'- and beta-subunits of beta-conglycinin can also serve as potential allergens. Immunoblot analysis using sera collected from soybean-allergic patients revealed the presence of IgE antibodies that recognized several soy proteins including 72, 70, 52, 34, and 21 kDa proteins. Matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF) analysis of trypsin-digested 72, 70, and 52 kDa proteins indicated that these proteins were the alpha'-, alpha-, and beta-subunits of beta-conglycinin, respectively. Additionally, purified alpha'-, alpha-, and beta-subunits of beta-conglycinin were recognized by IgE antibodies present in the soybean-allergic patients. The IgE reactivity to the beta-subunit of beta-conglycinin was not abolished when this glycoprotein was either deglycosylated using glycosidases or expressed as a recombinant protein in Escherichia coli . The results suggest that in addition to the previously recognized alpha-subunit of beta-conglycinin, the alpha'- and beta-subunits of beta-conglycinin also are potential food allergens.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Allergens,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Plant,
http://linkedlifedata.com/resource/pubmed/chemical/Globulins,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin E,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Subunits,
http://linkedlifedata.com/resource/pubmed/chemical/Seed Storage Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Soybean Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/beta-conglycinin protein, Glycine...
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1520-5118
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
11
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pubmed:volume |
57
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
938-43
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:19138084-Adult,
pubmed-meshheading:19138084-Allergens,
pubmed-meshheading:19138084-Amino Acid Sequence,
pubmed-meshheading:19138084-Antigens, Plant,
pubmed-meshheading:19138084-Food Hypersensitivity,
pubmed-meshheading:19138084-Globulins,
pubmed-meshheading:19138084-Humans,
pubmed-meshheading:19138084-Immunoblotting,
pubmed-meshheading:19138084-Immunoglobulin E,
pubmed-meshheading:19138084-Molecular Sequence Data,
pubmed-meshheading:19138084-Protein Subunits,
pubmed-meshheading:19138084-Seed Storage Proteins,
pubmed-meshheading:19138084-Seeds,
pubmed-meshheading:19138084-Soybean Proteins,
pubmed-meshheading:19138084-Soybeans
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pubmed:year |
2009
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pubmed:articleTitle |
All three subunits of soybean beta-conglycinin are potential food allergens.
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pubmed:affiliation |
U.S. Department of Agriculture, Division of Plant Sciences, Plant Genetics Research Unit, Agricultural Research Service, University of Missouri, Columbia, Missouri 65211, USA. Hari.Krishnan@ARS.USDA.GOV
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pubmed:publicationType |
Journal Article
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